Complementary roles of Fas-associated death domain (FADD) and receptor interacting protein kinase-3 (RIPK3) in T-cell homeostasis and antiviral immunity
出版年份 2011 全文链接
标题
Complementary roles of Fas-associated death domain (FADD) and receptor interacting protein kinase-3 (RIPK3) in T-cell homeostasis and antiviral immunity
作者
关键词
-
出版物
PROCEEDINGS OF THE NATIONAL ACADEMY OF SCIENCES OF THE UNITED STATES OF AMERICA
Volume 108, Issue 37, Pages 15312-15317
出版商
Proceedings of the National Academy of Sciences
发表日期
2011-08-30
DOI
10.1073/pnas.1102779108
参考文献
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注意:仅列出部分参考文献,下载原文获取全部文献信息。- FLIPLinduces caspase 8 activity in the absence of interdomain caspase 8 cleavage and alters substrate specificity
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- Inducible Dimerization and Inducible Cleavage Reveal a Requirement for Both Processes in Caspase-8 Activation
- (2010) Andrew Oberst et al. JOURNAL OF BIOLOGICAL CHEMISTRY
- Fas-associated death domain (FADD) is a negative regulator of T-cell receptor-mediated necroptosis
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- Receptor Interacting Protein Kinase-3 Determines Cellular Necrotic Response to TNF-α
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- RIP3, an Energy Metabolism Regulator That Switches TNF-Induced Cell Death from Apoptosis to Necrosis
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- Identification of a Molecular Signaling Network that Regulates a Cellular Necrotic Cell Death Pathway
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- Antigen-mediated T cell expansion regulated by parallel pathways of death
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- FADD and caspase-8 control the outcome of autophagic signaling in proliferating T cells
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